Characterization of a Novel, Low-molecular-weight DNA-binding Protein from Escherichia Coli

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1975 Sep 1

PMID 1103148

Citations 127

Authors

J Rouviere-Yaniv

F Gros

Affiliations

Soon will be listed here.

Abstract

A low-molecular-weight (7000), heat-stable protein--HU--that stimulates transcription of bacteriophage lambda DNA by E. coli RNA polymerase was purified from E. coli extracts using affinity chromatography on DNA-cellulose. HU binds to native DNA, resulting in an apparent thickening of the DNA chains as revealed by electron microscopy. Contrary to DNA unwinding proteins, it causes no destabilization of the double helix. HU differs from previously described transcription factors (H1, D, etc.) and from the low-molecular-weight omega subunit of the RNA polymerase. By its amino-acid composition and characteristics, HU displays an interesting resemblance to some eukaryotic histones, such as H2B and H1.

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